Extraordinary activation of CALB by alkylammonium ions: a new paradigm for activity enhancement of enzymes DOI
Rangasamy Savitha, Ebin K. Baby, Gemma K. Kinsella

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: April 20, 2025

Abstract Candida antarctica lipase B (CALB) is widely used in biocatalysis with applications plastics degradation and chemical synthesis. CALB activated by hydrophobic matrices and, enigmatically, shows striking activation polar, choline-based, Deep Eutectic Solvents (DES). Herein, we show that stabilisation TAAs caused binding to choline’s tetraalkylammonium (TAA) moiety. Several related TAA salts also which was proportional the hydrophobicity of their alkyl substituents. Remarkably, tetraoctylammonium bromide showed ∼500% even at low micromolar levels. These represent a new class enzyme activator. Molecular modelling identified alkylammonium location as patch centred around Asp-145 CALB. Binding this site explains polar DES solvents its relationship other pathways activation. demonstrate CALB, like many lipases, calcium. Intriguingly, mixed soluble activator experiments calcium choline bind different sites, suggesting two-site model for observations, along previous findings, widespread property enzymes constitutes novel potent means enhance turnover stability. Highlights cause Hyperactivation (5-fold) ions occurs concentrations. Two independent sites activation, ions, are Activation stabilises while destabilises A demonstrated, can be probe mechanism or enzymes.

Language: Английский

Efficient synthesis of isoamyl acetate in deep eutectic solvent utilizing in-situ aqueous phase immobilized lipase biocatalyst DOI
Yuyang Zhang, Qiujie Wang, Zhiyuan Lin

et al.

Food Bioscience, Journal Year: 2025, Volume and Issue: unknown, P. 105963 - 105963

Published: Jan. 1, 2025

Language: Английский

Citations

1
Extraordinary activation of CALB by alkylammonium ions: a new paradigm for activity enhancement of enzymes DOI
Rangasamy Savitha, Ebin K. Baby, Gemma K. Kinsella

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: April 20, 2025

Abstract Candida antarctica lipase B (CALB) is widely used in biocatalysis with applications plastics degradation and chemical synthesis. CALB activated by hydrophobic matrices and, enigmatically, shows striking activation polar, choline-based, Deep Eutectic Solvents (DES). Herein, we show that stabilisation TAAs caused binding to choline’s tetraalkylammonium (TAA) moiety. Several related TAA salts also which was proportional the hydrophobicity of their alkyl substituents. Remarkably, tetraoctylammonium bromide showed ∼500% even at low micromolar levels. These represent a new class enzyme activator. Molecular modelling identified alkylammonium location as patch centred around Asp-145 CALB. Binding this site explains polar DES solvents its relationship other pathways activation. demonstrate CALB, like many lipases, calcium. Intriguingly, mixed soluble activator experiments calcium choline bind different sites, suggesting two-site model for observations, along previous findings, widespread property enzymes constitutes novel potent means enhance turnover stability. Highlights cause Hyperactivation (5-fold) ions occurs concentrations. Two independent sites activation, ions, are Activation stabilises while destabilises A demonstrated, can be probe mechanism or enzymes.

Language: Английский

Citations

0